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3D 13C/1H NMR-based assignments for side-chain resonances of Lactobacillus casei dihydrofolate reductase. Evidence for similarities between the solution and crystal structures of the enzyme

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Summary

13C-based three-dimensional 1H−1H correlation experiments have been used to determine essentially complete 13C and 1H resonance assignments for the amino acid side chains of uniformly 13C/15N labelled L. casei dihydrofolate reductase in a complex with the drug methotrexate. Excellent agreement is observed between these assignments and an earlier set of partial assignments made on the basis of correlating nuclear Overhauser effect and crystal structure data, indicating that the tertiary structure of the enzyme is similar in solution and in the crystal state.

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Authors and Affiliations

  1. Laboratory of Molecular Structure, National Institute for Medical Research, Mill Hill, NW7 1AA, London, U.K.

    A. Soteriou, M. D. Carr, J. E. McCormick, D. Šali, B. Birdsall & J. Feeney

  2. MRC Biomedical NMR Centre, National Institute for Medical Research, Mill Hill, NW7 1AA, London, U.K.

    T. A. Frenkiel & C. J. Bauer

Authors
  1. A. Soteriou
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  2. M. D. Carr
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  3. T. A. Frenkiel
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  4. J. E. McCormick
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  5. C. J. Bauer
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  6. D. Šali
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  7. B. Birdsall
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  8. J. Feeney
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Soteriou, A., Carr, M.D., Frenkiel, T.A. et al. 3D 13C/1H NMR-based assignments for side-chain resonances of Lactobacillus casei dihydrofolate reductase. Evidence for similarities between the solution and crystal structures of the enzyme. J Biomol NMR 3, 535–546 (1993). https://doi.org/10.1007/BF00174608

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  • DOI: https://doi.org/10.1007/BF00174608

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